RENT1_MOUSE
ID RENT1_MOUSE Reviewed; 1124 AA.
AC Q9EPU0; Q3UG00; Q6GYP5; Q6PHQ5; Q8K0N4; Q99PR4;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Regulator of nonsense transcripts 1 {ECO:0000312|MGI:MGI:107995};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q92900};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q92900};
DE AltName: Full=ATP-dependent helicase RENT1 {ECO:0000303|PubMed:11152657};
DE AltName: Full=Nonsense mRNA reducing factor 1 {ECO:0000250|UniProtKB:Q92900};
DE Short=NORF1 {ECO:0000250|UniProtKB:Q92900};
DE AltName: Full=Up-frameshift suppressor 1 homolog;
DE Short=mUpf1;
GN Name=Upf1 {ECO:0000312|MGI:MGI:107995};
GN Synonyms=Rent1 {ECO:0000312|MGI:MGI:107995};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND DISRUPTION PHENOTYPE.
RC STRAIN=129/Sv;
RX PubMed=11152657; DOI=10.1093/hmg/10.2.99;
RA Medghalchi S.M., Frischmeyer P.A., Mendell J.T., Kelly A.G., Lawler A.M.,
RA Dietz H.C.;
RT "Rent1, a trans-effector of nonsense-mediated mRNA decay, is essential for
RT mammalian embryonic viability.";
RL Hum. Mol. Genet. 10:99-105(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Selg M., Strande J., Beck-Engeser G.B.J., Liehr T., Winkler T., Jack H.-M.;
RT "Genomic structure, chromosomal localization and expression of murine
RT nonsense mRNA reducing factor 1 (mNORF1).";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RC STRAIN=129/SvJ;
RA Selg M., Strande J.L., Liehr T., Roth E., Beck-Engeser G.B., Winkler T.H.,
RA Jack H.-M.;
RT "Cloning, genomic structure, chromosomal localization and expression of
RT mHUPF1, the murine homolog of the yeast nonsense mRNA reducing factor
RT UPF1.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, Embryo, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 73-1113 (ISOFORM 2).
RC STRAIN=129/Sv;
RX PubMed=8855285; DOI=10.1073/pnas.93.20.10928;
RA Perlick H.A., Medghalchi S.M., Spencer F.A., Kendzior R.J. Jr., Dietz H.C.;
RT "Mammalian orthologues of a yeast regulator of nonsense transcript
RT stability.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10928-10932(1996).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1102 AND SER-1105, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH UPF1 AND DDX4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=27149095; DOI=10.1371/journal.pgen.1005857;
RA Fanourgakis G., Lesche M., Akpinar M., Dahl A., Jessberger R.;
RT "Chromatoid Body Protein TDRD6 Supports Long 3' UTR Triggered Nonsense
RT Mediated mRNA Decay.";
RL PLoS Genet. 12:E1005857-E1005857(2016).
CC -!- FUNCTION: RNA-dependent helicase required for nonsense-mediated decay
CC (NMD) of aberrant mRNAs containing premature stop codons and modulates
CC the expression level of normal mRNAs (By similarity). Is recruited to
CC mRNAs upon translation termination and undergoes a cycle of
CC phosphorylation and dephosphorylation; its phosphorylation appears to
CC be a key step in NMD (By similarity). Recruited by release factors to
CC stalled ribosomes together with the SMG1C protein kinase complex to
CC form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex (By similarity).
CC In EJC-dependent NMD, the SURF complex associates with the exon
CC junction complex (EJC) (located 50-55 or more nucleotides downstream
CC from the termination codon) through UPF2 and allows the formation of an
CC UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD
CC (By similarity). Phosphorylated UPF1 is recognized by EST1B/SMG5, SMG6
CC and SMG7 which are thought to provide a link to the mRNA degradation
CC machinery involving exonucleolytic and endonucleolytic pathways, and to
CC serve as adapters to protein phosphatase 2A (PP2A), thereby triggering
CC UPF1 dephosphorylation and allowing the recycling of NMD factors (By
CC similarity). UPF1 can also activate NMD without UPF2 or UPF3, and in
CC the absence of the NMD-enhancing downstream EJC indicative for
CC alternative NMD pathways (By similarity). Plays a role in replication-
CC dependent histone mRNA degradation at the end of phase S; the function
CC is independent of UPF2 (By similarity). For the recognition of
CC premature termination codons (PTC) and initiation of NMD a competitive
CC interaction between UPF1 and PABPC1 with the ribosome-bound release
CC factors is proposed (By similarity). The ATPase activity of UPF1 is
CC required for disassembly of mRNPs undergoing NMD (By similarity).
CC Together with UPF2 and dependent on TDRD6, mediates the degradation of
CC mRNA harboring long 3'UTR by inducing the NMD machinery
CC (PubMed:27149095). Also capable of unwinding double-stranded DNA and
CC translocating on single-stranded DNA (By similarity).
CC {ECO:0000250|UniProtKB:Q92900, ECO:0000269|PubMed:27149095}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q92900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q92900};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:Q92900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q92900};
CC -!- SUBUNIT: Found in a post-splicing messenger ribonucleoprotein (mRNP)
CC complex. Associates with the exon junction complex (EJC). Associates
CC with the SGM1C complex; is phosphorylated by the complex kinase
CC component SGM1. Part of a complex composed of SMG1, DHX34 and UPF1;
CC within the complex DHX34 acts as a scaffolding protein to facilitate
CC SMG1 phosphorylation of UPF1 (By similarity). Interacts with UPF2.
CC Interacts with UPF3A and UPF3B. Interacts with EST1A. Interacts with
CC SLBP. Interacts (when hyperphosphorylated) with PNRC2. Interacts with
CC AGO1 and AGO2. Interacts with GSPT2. Interacts with isoform 1 and
CC isoform 5 of ADAR/ADAR1. Interacts with SMG7. Interacts with ZC3H12A;
CC this interaction occurs in a mRNA translationally active- and
CC termination-dependent manner and is essential for ZC3H12A-mediated
CC degradation of target mRNAs. Interacts with CPSF6. Interacts with
CC MOV10; the interaction is direct and RNA-dependent. Interacts with
CC SHFL; the interaction increases in the presence of RNA. Interacts with
CC UPF2 and DDX4; interactions are mediated by TDRD6 (PubMed:27149095).
CC Interacts with DHX34 and PABPC1/PABP1; the interactions are RNA-
CC independent (By similarity). {ECO:0000250|UniProtKB:Q92900,
CC ECO:0000269|PubMed:27149095}.
CC -!- INTERACTION:
CC Q9EPU0; Q7TMF2: Eri1; NbExp=2; IntAct=EBI-6876715, EBI-16026214;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27149095}.
CC Cytoplasm, P-body {ECO:0000250|UniProtKB:Q92900}. Nucleus
CC {ECO:0000250|UniProtKB:Q92900}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:27149095}. Note=Hyperphosphorylated form is
CC targeted to the P-body, while unphosphorylated protein is distributed
CC throughout the cytoplasm (By similarity). Localized in the chromatoid
CC bodies of round spermatids (PubMed:27149095).
CC {ECO:0000250|UniProtKB:Q92900, ECO:0000269|PubMed:27149095}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9EPU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EPU0-2; Sequence=VSP_025764;
CC -!- TISSUE SPECIFICITY: Localizes in male germ cells.
CC {ECO:0000269|PubMed:27149095}.
CC -!- DEVELOPMENTAL STAGE: Weakly expressed in neonatal testes and expression
CC increases during the development of spermatocytes and spermatids, in
CC the late meiotic and postmeiotic stages of spermatogenesis.
CC {ECO:0000269|PubMed:27149095}.
CC -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC from the PI3/PI4-kinase family. {ECO:0000250|UniProtKB:Q92900}.
CC -!- PTM: Phosphorylated by SMG1; required for formation of mRNA
CC surveillance complexes. {ECO:0000250|UniProtKB:Q92900}.
CC -!- DISRUPTION PHENOTYPE: Embryos are viable in pre-implantation period,
CC show complete loss of NMD but are resorbed shortly after implantation.
CC {ECO:0000269|PubMed:11152657}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR EMBL; AF322655; AAG42830.1; -; mRNA.
DR EMBL; AY597039; AAT46119.1; -; Genomic_DNA.
DR EMBL; AY597038; AAT46119.1; JOINED; Genomic_DNA.
DR EMBL; AK148196; BAE28409.1; -; mRNA.
DR EMBL; BC030916; AAH30916.1; -; mRNA.
DR EMBL; BC052149; AAH52149.1; -; mRNA.
DR EMBL; BC056442; AAH56442.1; -; mRNA.
DR EMBL; AF182947; AAK08652.1; -; mRNA.
DR CCDS; CCDS52572.1; -. [Q9EPU0-1]
DR CCDS; CCDS90409.1; -. [Q9EPU0-2]
DR RefSeq; NP_001116301.1; NM_001122829.2. [Q9EPU0-1]
DR RefSeq; NP_109605.2; NM_030680.3. [Q9EPU0-2]
DR RefSeq; XP_006509667.1; XM_006509604.3. [Q9EPU0-1]
DR RefSeq; XP_006509668.1; XM_006509605.3. [Q9EPU0-1]
DR AlphaFoldDB; Q9EPU0; -.
DR SMR; Q9EPU0; -.
DR BioGRID; 202860; 54.
DR DIP; DIP-60114N; -.
DR IntAct; Q9EPU0; 11.
DR MINT; Q9EPU0; -.
DR STRING; 10090.ENSMUSP00000075089; -.
DR iPTMnet; Q9EPU0; -.
DR PhosphoSitePlus; Q9EPU0; -.
DR SwissPalm; Q9EPU0; -.
DR EPD; Q9EPU0; -.
DR jPOST; Q9EPU0; -.
DR MaxQB; Q9EPU0; -.
DR PaxDb; Q9EPU0; -.
DR PeptideAtlas; Q9EPU0; -.
DR PRIDE; Q9EPU0; -.
DR ProteomicsDB; 253209; -. [Q9EPU0-1]
DR ProteomicsDB; 253210; -. [Q9EPU0-2]
DR Antibodypedia; 15175; 353 antibodies from 37 providers.
DR DNASU; 19704; -.
DR Ensembl; ENSMUST00000075666; ENSMUSP00000075089; ENSMUSG00000058301. [Q9EPU0-1]
DR Ensembl; ENSMUST00000215817; ENSMUSP00000148927; ENSMUSG00000058301. [Q9EPU0-2]
DR GeneID; 19704; -.
DR KEGG; mmu:19704; -.
DR UCSC; uc009mab.2; mouse. [Q9EPU0-1]
DR UCSC; uc012gfa.1; mouse. [Q9EPU0-2]
DR CTD; 5976; -.
DR MGI; MGI:107995; Upf1.
DR VEuPathDB; HostDB:ENSMUSG00000058301; -.
DR eggNOG; KOG1802; Eukaryota.
DR GeneTree; ENSGT00940000157413; -.
DR HOGENOM; CLU_001666_4_3_1; -.
DR InParanoid; Q9EPU0; -.
DR OMA; HHDSIGY; -.
DR OrthoDB; 62494at2759; -.
DR PhylomeDB; Q9EPU0; -.
DR TreeFam; TF300554; -.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 19704; 26 hits in 113 CRISPR screens.
DR ChiTaRS; Upf1; mouse.
DR PRO; PR:Q9EPU0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9EPU0; protein.
DR Bgee; ENSMUSG00000058301; Expressed in floor plate of midbrain and 188 other tissues.
DR Genevisible; Q9EPU0; MM.
DR GO; GO:0000785; C:chromatin; ISS:HGNC-UCL.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044530; C:supraspliceosomal complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:HGNC-UCL.
DR GO; GO:0036121; F:double-stranded DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0044770; P:cell cycle phase transition; ISS:HGNC.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:HGNC-UCL.
DR GO; GO:0006260; P:DNA replication; ISS:HGNC-UCL.
DR GO; GO:0071044; P:histone mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; ISO:MGI.
DR GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; ISS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0032204; P:regulation of telomere maintenance; ISO:MGI.
DR GO; GO:0006449; P:regulation of translational termination; ISS:HGNC-UCL.
DR GO; GO:0032201; P:telomere maintenance via semi-conservative replication; ISO:MGI.
DR CDD; cd21407; 1B_UPF1-like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR CDD; cd21400; ZBD_UPF1-like; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040812; UPF1_1B_dom.
DR InterPro; IPR018999; UPF1_CH/ZBD.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF18141; UPF1_1B_dom; 1.
DR Pfam; PF09416; UPF1_Zn_bind; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51997; UPF1_CH_RICH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Helicase; Hydrolase;
KW Metal-binding; Methylation; Nonsense-mediated mRNA decay;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..1124
FT /note="Regulator of nonsense transcripts 1"
FT /id="PRO_0000080717"
FT DOMAIN 110..267
FT /note="Upf1 CH-rich"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 1..410
FT /note="Sufficient for interaction with RENT2"
FT /evidence="ECO:0000250"
FT REGION 39..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..150
FT /note="C3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 132..160
FT /note="CC/SHH/C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 178..208
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 1004..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1084..1085
FT /note="[ST]-Q motif 1"
FT MOTIF 1102..1103
FT /note="[ST]-Q motif 2"
FT COMPBIAS 1032..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 501..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 671
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 708
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 839
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT MOD_RES 1014
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT MOD_RES 1084
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT MOD_RES 1102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT VAR_SEQ 348..358
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11152657,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8855285,
FT ECO:0000303|Ref.2"
FT /id="VSP_025764"
FT CONFLICT 56
FT /note="G -> S (in Ref. 3; AAT46119)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="G -> A (in Ref. 4; BAE28409)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="A -> P (in Ref. 3; AAT46119)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="A -> S (in Ref. 3; AAT46119)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="R -> K (in Ref. 3; AAT46119)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="D -> E (in Ref. 3; AAT46119)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="V -> F (in Ref. 3; AAT46119)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="L -> F (in Ref. 3; AAT46119)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="K -> E (in Ref. 4; BAE28409)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="H -> Y (in Ref. 4; BAE28409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1124 AA; 123967 MW; 5F1B0ED50F63C52E CRC64;
MSVEAYGPSS QTLTFLDTEE AELLGADTQG SEFEFTDFTL PSQTQTPPGG PGGAGGPGGA
GAGGAAGQLD AQVGPEGILQ NGAVDDSVAK TSQLLAELNF EEDEEDTYYT KDLPVHACSY
CGIHDPACVV YCNTSKKWFC NGRGNTSGSH IVNHLVRAKC KEVTLHKDGP LGETVLECYN
CGCRNVFLLG FIPAKADSVV VLLCRQPCAS QSSLKDINWD SSQWQPLIQD RCFLSWLVKI
PSEQEQLRAR QITAQQINKL EELWKENPSA TLEDLEKPGV DEEPQHVLLR YEDAYQYQNI
FGPLVKLEAD YDKKLKESQT QDNITVRWDL GLNKKRIAFF TLPKTDSGNE DLVIIWLRDM
RLMQGDEICL RYKGDLAPLW KGIGHVIKVP DNYGDEIAIE LRSSVGAPVE VTHNFQVDFV
WKSTSFDRMQ SALKTFAVDE TSVSGYIYHK LLGHEVEDVV IKCQLPKRFT AQGLPDLNHS
QVYAVKTVLQ RPLSLIQGPP GTGKTVTSAT IVYHLARQGN GPVLVCAPSN IAVDQLTEKI
HQTGLKVVRL CAKSREAIDS PVSFLALHNQ IRNMDSMPEL QKLQQLKDET GELSSADEKR
YRALKRTAER ELLMNADVIC CTCVGAGDPR LAKMQFRSIL IDESTQATEP ECMVPVVLGA
KQLILVGDHC QLGPVVMCKK AAKAGLSQSL FERLVVLGIR PIRLQVQYRM HPALSAFPSN
IFYEGSLQNG VTAADRVKKG FDFQWPQPDK PMFFYVTQGQ EEIASSGTSY LNRTEAANVE
KITTKLLKAG AKPDQIGIIT PYEGQRSYLV QYMQFSGSLH TKLYQEVEIA SVDAFQGREK
DFIILSCVRA NEHQGIGFLN DPRRLNVALT RARYGVIIVG NPKALSKQPL WNHLLSYYKE
QKALVEGPLN NLRESLMQFS KPRKLVNTVN PGARFMTTAM YDAREAIIPG SVYDRSSQGR
PSNMYFQTHD QISMISAGPS HVAAMNIPIP FNLVMPPMPP PGYFGQANGP AAGRGTPKTK
TGRGGRQKNR FGLPGPSQTT LPNSQASQDV ASQPFSQGAL TQGYVSMSQP SQMSQPGLSQ
PELSQDSYLG DEFKSQIDVA LSQDSTYQGE RAYQHGGVTG LSQY
